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Volumn 240, Issue 1, 1996, Pages 274-279

Tetrameric and octameric lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima Structure and stability of the two active forms

Author keywords

Hyperthermophiles; Lactate dehydrogenase; Quaternary structure; Stability; Thermotoga maritima

Indexed keywords

LACTATE DEHYDROGENASE;

EID: 0029822814     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0274h.x     Document Type: Article
Times cited : (22)

References (3)
  • 1
    • 0019883136 scopus 로고
    • Reversible solvent denaturation of rabbit muscle pyruvate dehydrogenase
    • Doster, W. & Hess, B. (1981) Reversible solvent denaturation of rabbit muscle pyruvate dehydrogenase. Biochemistry 20, 772-780.
    • (1981) Biochemistry , vol.20 , pp. 772-780
    • Doster, W.1    Hess, B.2
  • 2
    • 0015903106 scopus 로고
    • Lactate dehydrogenase: Electro-phoretic behavior, electron microscopy and structure
    • Dudman, N. P. B. & Zerner, B. (1973) Lactate dehydrogenase: electro-phoretic behavior, electron microscopy and structure, Biochim. Biophys. Acta 310, 248-263.
    • (1973) Biochim. Biophys. Acta , vol.310 , pp. 248-263
    • Dudman, N.P.B.1    Zerner, B.2
  • 3
    • 0020484055 scopus 로고
    • Partial specific volume changes of proteins: Densimetric studies
    • Durchschlag, H. &Jaenicke, R. (1982) Partial specific volume changes of proteins: densimetric studies, Biochem. Biophys. Res. Commun. 108, 1074-1079.
    • (1982) Biochem. Biophys. Res. Commun. , vol.108 , pp. 1074-1079
    • Durchschlag, H.1    Jaenicke, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.